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Conserved domains on  [gi|31563512|ref|NP_852668|]
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N-alpha-acetyltransferase 20 isoform b [Homo sapiens]

Protein Classification

GNAT family N-acetyltransferase( domain architecture ID 10456837)

GNAT family N-acetyltransferase catalyzes the transfer of an acetyl group from acetyl-CoA to a substrate

CATH:  3.40.630.30
EC:  2.3.-.-
Gene Ontology:  GO:0016746|GO:0008080
SCOP:  3000403

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-116 1.24e-17

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


:

Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 74.09  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    13 ETYGIPFYLQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKG 92
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92
                          90       100
                  ....*....|....*....|....
gi 31563512    93 GFFVDLFVRVSNQVAVNMYKQLGY 116
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLGF 116
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-116 1.24e-17

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 74.09  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    13 ETYGIPFYLQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKG 92
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92
                          90       100
                  ....*....|....*....|....
gi 31563512    93 GFFVDLFVRVSNQVAVNMYKQLGY 116
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
43-145 5.77e-17

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  43 GYIMGkaegSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTV 122
Cdd:COG0456   1 GFALL----GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
                        90       100
                ....*....|....*....|...
gi 31563512 123 IEYYsasngepDEDAYDMRKALS 145
Cdd:COG0456  77 PNYY-------GDDALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
10-140 1.28e-14

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 66.58  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    10 PLTETYGIPFYLQYLAHWpeyfIVAEApGGELMGYIMGkaegSVAREEwhGHVTALSVAPEFRRLGLAAKLMELLEEISE 89
Cdd:TIGR01575  16 PWTEAQFAEELANYHLCY----LLARI-GGKVVGYAGV----QIVLDE--AHILNIAVKPEYQGQGIGRALLRELIDEAK 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 31563512    90 RKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSasngEPDEDAYDM 140
Cdd:TIGR01575  85 GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
24-118 2.14e-12

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 60.71  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512   24 LAHWPEYFIVAEApGGELMGYIMGKAEGsvareewH-GHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRV 102
Cdd:PRK03624  40 LNHDPSLFLVAEV-GGEVVGTVMGGYDG-------HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVRE 111
                         90
                 ....*....|....*.
gi 31563512  103 SNQVAVNMYKQLGYSV 118
Cdd:PRK03624 112 DNDAVLGFYEALGYEE 127
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
31-98 8.19e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.89  E-value: 8.19e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563512  31 FIVAEApGGELMGYIMGKAEGSVAReewHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDL 98
Cdd:cd04301   1 FLVAED-DGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
 
Name Accession Description Interval E-value
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
13-116 1.24e-17

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 74.09  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    13 ETYGIPFYLQYLAHWPEYFIVAEApGGELMGYIMGKAEGsvaREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKG 92
Cdd:pfam00583  17 PDEPLDLLEDWDEDASEGFFVAEE-DGELVGFASLSIID---DEPPVGEIEGLAVAPEYRGKGIGTALLQALLEWARERG 92
                          90       100
                  ....*....|....*....|....
gi 31563512    93 GFFVDLFVRVSNQVAVNMYKQLGY 116
Cdd:pfam00583  93 CERIFLEVAADNLAAIALYEKLGF 116
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
43-145 5.77e-17

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 71.61  E-value: 5.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  43 GYIMGkaegSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTV 122
Cdd:COG0456   1 GFALL----GLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEAAIALYEKLGFEEVGER 76
                        90       100
                ....*....|....*....|...
gi 31563512 123 IEYYsasngepDEDAYDMRKALS 145
Cdd:COG0456  77 PNYY-------GDDALVMEKELA 92
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
10-140 1.28e-14

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 66.58  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    10 PLTETYGIPFYLQYLAHWpeyfIVAEApGGELMGYIMGkaegSVAREEwhGHVTALSVAPEFRRLGLAAKLMELLEEISE 89
Cdd:TIGR01575  16 PWTEAQFAEELANYHLCY----LLARI-GGKVVGYAGV----QIVLDE--AHILNIAVKPEYQGQGIGRALLRELIDEAK 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 31563512    90 RKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSasngEPDEDAYDM 140
Cdd:TIGR01575  85 GRGVNEIFLEVRVSNIAAQALYKKLGFNEIAIRRNYYP----DPGEDAIVM 131
PRK03624 PRK03624
putative acetyltransferase; Provisional
24-118 2.14e-12

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 60.71  E-value: 2.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512   24 LAHWPEYFIVAEApGGELMGYIMGKAEGsvareewH-GHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRV 102
Cdd:PRK03624  40 LNHDPSLFLVAEV-GGEVVGTVMGGYDG-------HrGWAYYLAVHPDFRGRGIGRALVARLEKKLIARGCPKINLQVRE 111
                         90
                 ....*....|....*.
gi 31563512  103 SNQVAVNMYKQLGYSV 118
Cdd:PRK03624 112 DNDAVLGFYEALGYEE 127
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
51-125 1.03e-09

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 52.60  E-value: 1.03e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 31563512  51 GSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGYSVYRTVIEY 125
Cdd:COG3393   7 GVRAESPGVAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDADNPAARRLYERLGFRPVGEYATV 81
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
29-118 2.95e-09

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 51.30  E-value: 2.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    29 EYFIVAEApGGELMGYIMGKAEGSVAREEWHGhvtaLSVAPEFRRLGLAAKLMELLEEISERKGgffVDLFVRVSNQVAV 108
Cdd:pfam13508   3 GRFFVAED-DGKIVGFAALLPLDDEGALAELR----LAVHPEYRGQGIGRALLEAAEAAAKEGG---IKLLELETTNRAA 74
                          90
                  ....*....|
gi 31563512   109 NMYKQLGYSV 118
Cdd:pfam13508  75 AFYEKLGFEE 84
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
30-144 1.34e-08

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 51.15  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  30 YFIVAEApGGELMGYimgkAEGSVAREEWHGHVTA---LSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQV 106
Cdd:COG1247  53 PVLVAEE-DGEVVGF----ASLGPFRPRPAYRGTAeesIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEA 127
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 31563512 107 AVNMYKQLGYSVYRTVIEYYSASNGEPDEdaYDMRKAL 144
Cdd:COG1247 128 SIALYEKLGFEEVGTLPEVGFKFGRWLDL--VLMQKRL 163
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
28-144 2.01e-08

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 50.47  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  28 PEYFIVAEApGGELMGYIMGkAEGSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGgffVDLFVRVSNQVA 107
Cdd:COG3153  38 AGLSLVAED-DGEIVGHVAL-SPVDIDGEGPALLLGPLAVDPEYRGQGIGRALMRAALEAARERG---ARAVVLLGDPSL 112
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 31563512 108 VNMYKQLGYSVYRTVieyysasNGEPDEDAYDMRKAL 144
Cdd:COG3153 113 LPFYERFGFRPAGEL-------GLTLGPDEVFLAKEL 142
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
31-98 8.19e-08

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 46.89  E-value: 8.19e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31563512  31 FIVAEApGGELMGYIMGKAEGSVAReewHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDL 98
Cdd:cd04301   1 FLVAED-DGEIVGFASLSPDGSGGD---TAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLRL 64
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
30-116 1.34e-07

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 47.65  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512    30 YFIVAEApGGELMGYImgkaegSVAReewHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQvAVN 109
Cdd:pfam13673  32 FFFVAFE-GGQIVGVI------ALRD---RGHISLLFVDPDYQGQGIGKALLEAVEDYAEKDGIKLSELTVNASPY-AVP 100

                  ....*..
gi 31563512   110 MYKQLGY 116
Cdd:pfam13673 101 FYEKLGF 107
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
29-125 1.36e-07

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 48.13  E-value: 1.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  29 EYFIVAEApGGELMGYIMGKAEGsvareEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAV 108
Cdd:COG0454  34 AEFIAVDD-KGEPIGFAGLRRLD-----DKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDGNPAAI 107
                        90
                ....*....|....*..
gi 31563512 109 NMYKQLGYSVYRTVIEY 125
Cdd:COG0454 108 RFYERLGFKEIERYVAY 124
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
67-145 1.63e-07

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 47.87  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  67 VAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSnqvAVNMYKQLGYSVYrtvieyysasnGEPDEDA----YDMRK 142
Cdd:COG2153  66 VLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAH---AVGFYEKLGFVPV-----------GEEFLEAgiphIDMRK 131

                ...
gi 31563512 143 ALS 145
Cdd:COG2153 132 PLS 134
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
31-118 3.93e-07

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 46.52  E-value: 3.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  31 FIVAEApGGELMGYImgkaeGSVAREEWHGHVTALSVAPEFRRLGLAAKLMELLEEISERKGgfFVDLFVrVSNQVAVNM 110
Cdd:COG1246  30 FWVAEE-DGEIVGCA-----ALHPLDEDLAELRSLAVHPDYRGRGIGRRLLEALLAEARELG--LKRLFL-LTTSAAIHF 100

                ....*...
gi 31563512 111 YKQLGYSV 118
Cdd:COG1246 101 YEKLGFEE 108
rimI PRK09491
ribosomal-protein-alanine N-acetyltransferase; Provisional
65-140 1.31e-06

ribosomal-protein-alanine N-acetyltransferase; Provisional


Pssm-ID: 181904 [Multi-domain]  Cd Length: 146  Bit Score: 45.31  E-value: 1.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 31563512   65 LSVAPEFRRLGLAAKLMELLEEISERKGGFFVDLFVRVSNQVAVNMYKQLGY---SVYRtviEYYSASNGEpdEDAYDM 140
Cdd:PRK09491  69 IAVDPDYQRQGLGRALLEHLIDELEKRGVATLWLEVRASNAAAIALYESLGFnevTIRR---NYYPTADGR--EDAIIM 142
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
60-121 3.40e-05

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 40.39  E-value: 3.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 31563512    60 GHVTALSVAPEFRRLGLAAKLM-ELLEEISERkgGFFVDLFVRVSNQVAVNMYKQLGYSVYRT 121
Cdd:pfam08445  22 GELGALQTLPEHRRRGLGSRLVaALARGIAER--GITPFAVVVAGNTPSRRLYEKLGFRKIDE 82
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
19-143 4.46e-05

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 41.52  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31563512  19 FYLQYLAHWPE----YFIVAEAPGGELMGYImgkaegSVAREEWHGHVT--ALSVAPEFRRLGLAAKLMELLEEISERKG 92
Cdd:COG1670  47 WLERLLADWADggalPFAIEDKEDGELIGVV------GLYDIDRANRSAeiGYWLAPAYWGKGYATEALRALLDYAFEEL 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 31563512  93 GF-FVDLFVRVSNQVAVNMYKQLGYSVYRTVIEYYSASNGEPDEDAYDMRKA 143
Cdd:COG1670 121 GLhRVEAEVDPDNTASIRVLEKLGFRLEGTLRDALVIDGRYRDHVLYSLLRE 172
Eis COG4552
Predicted acetyltransferase [General function prediction only];
60-90 1.43e-03

Predicted acetyltransferase [General function prediction only];


Pssm-ID: 443616 [Multi-domain]  Cd Length: 393  Bit Score: 37.96  E-value: 1.43e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 31563512  60 GHVTALSVAPEFRRLGLAAKLM-ELLEEISER 90
Cdd:COG4552  73 AGITGVAVAPEHRRRGVARALLrEALAELRER 104
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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